Glycoproteins in prokaryotes

Arch Microbiol. 1997 Sep;168(3):169-75. doi: 10.1007/s002030050484.


Rather recently it has become clear that prokaryotes (Archaea and Bacteria) are able to glycosylate proteins. A literature survey revealed the different types of glycoproteins. They include mainly surface layer (S-layer) proteins, flagellins, and polysaccharide-degrading enzymes. Only in a few cases is structural information available. Many different structures have been observed that display much more variation than that observed in eukaryotes. A few studies have given evidence for the function of the prokaryotic glycoprotein glycans. Also from the biosynthetic point of view, information is rather scarce. Due to their different cell structure, prokaryotes have to use mechanisms different from those found in eukaryotes to glycosylate proteins. However, from the fragmented data available for the prokaryotic glycoproteins, similarities with the eukaryotic system can be noticed.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Archaea / chemistry
  • Archaea / metabolism
  • Archaeal Proteins / chemistry
  • Archaeal Proteins / metabolism
  • Bacteria / chemistry
  • Bacteria / metabolism*
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism*
  • Glycoproteins / chemistry
  • Glycoproteins / metabolism*
  • Glycosylation
  • Membrane Glycoproteins / chemistry
  • Membrane Glycoproteins / metabolism*
  • Prokaryotic Cells / chemistry
  • Prokaryotic Cells / metabolism
  • Protein Processing, Post-Translational*


  • Archaeal Proteins
  • Bacterial Proteins
  • Glycoproteins
  • Membrane Glycoproteins